Abstract
Two glutathione S-transferase isozymes from the mosquito Anopheles dirus (AdGST1-3 and AdGST1-4) from an alternately spliced gene family have been expressed, purified and crystallized. The isozymes share an N-terminal domain derived from a single exon and C-terminal domains from unique exons. Despite the high level of sequence identity (64% overall), the two isozymes crystallize in different space groups, the 1-3 isozyme in P3121 or P3221 (unit-cell parameters a = 49.9, c = 271.8 Å at 100 K) and the 1-4 isozyme in P41 or P43 (unit-cell parameters a = 87.8, c = 166.1 at 100 K). Determination of these structures will advance our understanding of how these enzymes inactivate pesticides and the structural consequences of alternate splicing.
Original language | English |
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Pages (from-to) | 870-872 |
Number of pages | 3 |
Journal | Acta Crystallographica Section D: Biological Crystallography |
Volume | 57 |
Issue number | 6 |
DOIs | |
Publication status | Published - 4 Jul 2001 |
Externally published | Yes |